Isomerization of glucose to fructose. 2. Optimization of reaction conditions in the production of high fructose syrup by isomerization of glucose catalyzed by a whole cell immobilized glucose isomerase catalyst

Straatsma, J.; Vellenga, K.; Wilt, H.G.J. de; Joosten, G.E.H.

doi:10.1021/i200022a003

Cited by 18 publications

(17 citation statements)

References 3 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…On the whole the literature (Straatsma et at., 1983; 0.0.-0.0 Vos et al, 1990;Jurado et al, 1994) reports that the kinetic of the reaction is close to a pseudo-first-order one: rr~ = k°pso(xe -x) (12) where xe represents the equilibrium conversion and kop includes the concentration of the active enzyme per gram of enzymatic compound. Integrating eq.…”

Section: Characterization Of the Immobilized Enzyme Particlesmentioning

confidence: 99%

A comparative study of the activity of free and immobilized enzymes and its application to glucose isomerase

Camacho-Rubio

Alameda

González-Tello

et al. 1996

Chemical Engineering Science

View full text Add to dashboard Cite

Abstract--We have made an experimental study of the isomerization of fructose and glucose by glucose isomerase in two forms: one soluble and the other immobilized by being fixed in a gel matrix. For the latter technique we used a fixed-bed differential reeirculation reactor, which allowed us to obtain comparable results to those we got with the enzyme dissolved within a batch reactor. We propose a simple method of comparing the results obtained in both systems, which permits us to determine the relative activity of each enzyme and also the effective diffusivity in the immobilized enzyme. The values obtained for the latter indicate a tortuosity factor of 2.04, which is lower than that generally found in porous solids but consistent with the results published in the literature for diffusion in gel particles.The application of our method to the results arrived at with the two systems studied confirms the validity of the kinetic model for glucose-fructose isomerization and has lead to our being able to determine both the kinetic constants for the reaction and their variation according to temperature.

show abstract

Section: Characterization Of the Immobilized Enzyme Particlesmentioning

confidence: 99%

A comparative study of the activity of free and immobilized enzymes and its application to glucose isomerase

Camacho-Rubio

Alameda

González-Tello

et al. 1996

Chemical Engineering Science

View full text Add to dashboard Cite

show abstract

“…A simpler purification process, based on isomerases immobilized on solid supports after the hydrolysis reaction were reported. Such processes have the advantage of reutilizing the isomerase [5], [6].…”

Section: Introductionmentioning

confidence: 99%

Kinetics of a Three-Step Isomerization of Glucose to Fructose Using Immobilized Enzyme

Gaily¹,

Sulieman²,

Abasaeed³

2013

IJCEA

View full text Add to dashboard Cite

Abstract-A three-step complex formation of fructose by glucose isomerization was suggested to describe the isomerization kinetics. The model was characterized by the formation of a fructose complex. Experimental data obtained from the isomerization process using immobilized Sweetzyme enzyme, IT® were used in this study. Experiments were conducted at different reaction temperatures in the range of 50-70°C and glucose initial concentrations of 10, 15 and 20% and enzyme loading of 1g. Glucose concentrations dropped with time until equilibrium was reached. A first order kinetics for the steps was employed and Runge Kutta 4th order algorithm combined with a least square method were used to estimate the pre-experimental factor and activation energy for determination of the corresponding rate constants by solving the initial value problem of the suggested model using EZ-Solve software. Very good fits between experimental data and model prediction was obtained.

show abstract

“…The ®rst one is the control of feed rate to the reactor in such a way that it decreases as function of time in order to compensate for the loss of enzyme activity. The second mode is the temperature and/or pH pro®le that is set according to a well-de®ned time pro®le (Faqir, 1998;Haas et al, 1974;Kim et al, 1982;Park et al, 1981;Straatsma et al, 1983;Vos and Luyben, 1993). Temperature is one of the most important variables due to its eect on the kinetic parameters, enzyme activity, and substrate protection factor.…”

Section: Introductionmentioning

confidence: 99%

“…However, one limitation of this control variable is the narrow range within which enzymes remain active (Lee, 1992). In spite of this, many researchers have used two types of temperature operating policies utilizing the enzymatic isomerization of glucose to fructose as a model system (Abu-Reesh and Faqir, 1996;Faqir, 1998;Hass et al, 1974;Kim et al, 1982;Park et al, 1981;Straatsma et al, 1983). These operating policies are either a rising temperature policy with time to maintain a constant outlet conversion or a constant temperature pro®le that maximizes the average reactor productivity.…”

Section: Introductionmentioning

confidence: 99%

“…Most of the published works on determining the optimum temperature operating policy for continuous packed bed reactors performing reversible Michaelis±Menten kinetics use either Pontryagin's maximum principle or nonlinear programming methods (Faqir, 1998;Haas et al, 1974;Kim et al, 1982;Park et al, 1981;Straatsma et al, 1983;Vos and Luyben, 1993). The main disadvantages of these optimization methods are the tedious formulation and complex solution algorithms used to obtain the desired solution.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Optimal temperature policy for immobilized enzyme packed bed reactor performing reversible Michaelis–Menten kinetics using the disjoint policy

Faqir¹,

Attarakih²

2001

Biotech & Bioengineering

View full text Add to dashboard Cite

The optimal temperature policy that maximizes the time-averaged productivity of a continuous immobilized enzyme packed bed reactor is determined. This optimization study takes into consideration the enzyme thermal deactivation with substrate protection during the reactor operation. The general case of reversible Michaelis-Menten kinetics under constant reactor feed flow rate is assumed. The corresponding nonlinear optimization problem is solved using the calculus of variations by applying the disjoint policy. This policy reduces the optimization problem into a differential-algebraic system, DAE. This DAE system defines completely the optimal temperature-time profiles. These profiles depend on the kinetic parameters, feed substrate concentration, operating period, and the residence time and are characterized by increasing form with time. Also, general analytical expressions for the slopes of the temperature and residual enzyme activity profiles are derived. An efficient solution algorithm is developed to solve the DAE system, which results into a one-dimensional optimization problem with simple bounds on the initial feed temperature. The enzymatic isomerization of glucose into fructose is selected as a case study. The computed productivities are very close to that obtained by numerical nonlinear optimization with simpler problem to solve. Moreover, the computed conversion profiles are almost constant over 90% of the operating periods, thus producing a homogeneous product.

show abstract

Isomerization of glucose to fructose. 2. Optimization of reaction conditions in the production of high fructose syrup by isomerization of glucose catalyzed by a whole cell immobilized glucose isomerase catalyst

Cited by 18 publications

References 3 publications

A comparative study of the activity of free and immobilized enzymes and its application to glucose isomerase

A comparative study of the activity of free and immobilized enzymes and its application to glucose isomerase

Kinetics of a Three-Step Isomerization of Glucose to Fructose Using Immobilized Enzyme

Optimal temperature policy for immobilized enzyme packed bed reactor performing reversible Michaelis–Menten kinetics using the disjoint policy

Contact Info

Product

Resources

About